|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1-288 |
4.20e-173 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 486.17 E-value: 4.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07103 165 ELAEEAGLPAGVLNVVTG-SPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDK 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07103 244 AVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:cd07103 324 KVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEA 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 241 LEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07103 404 LEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
3-289 |
4.58e-142 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 408.36 E-value: 4.58e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:COG1012 191 LEEAGLPAGVLNVVTG-DGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:COG1012 270 EAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDG-PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGL 241
Cdd:COG1012 350 LTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRL 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 652636290 242 EFGLMGFNSGVIS-NAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGIQ 289
Cdd:COG1012 430 EAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
4-286 |
2.58e-139 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 402.15 E-value: 2.58e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 4 LDAGLPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVE 83
Cdd:PLN02278 211 LQAGIPPGVLNVVMGD-APEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 84 GAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:PLN02278 290 GALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:PLN02278 370 LGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEY 449
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 652636290 244 GLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:PLN02278 450 GIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
6-284 |
1.42e-133 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 386.02 E-value: 1.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGKSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:TIGR01780 170 AGIPKGVLNVITGSRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDADLDQAVEGA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:TIGR01780 250 MASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAVEKGAKVVTG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGL 245
Cdd:TIGR01780 330 GKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWRVAEALEYGM 409
|
250 260 270
....*....|....*....|....*....|....*....
gi 652636290 246 MGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQ 284
Cdd:TIGR01780 410 VGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
3-286 |
2.53e-128 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 373.02 E-value: 2.53e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSASaISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:pfam00171 176 FEEAGLPAGVLNVVTGSGAE-VGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:pfam00171 255 EAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:pfam00171 335 LTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLE 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 243 FGLMGFNSGVISNA-AAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:pfam00171 415 AGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1-286 |
6.67e-121 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 353.05 E-value: 6.67e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07078 144 ELLAEAGLPPGVLNVVTG-DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07078 223 AVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDG-PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSD 239
Cdd:cd07078 303 KLLCGGKRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAE 382
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 240 GLEFGLMGFN-SGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07078 383 RLEAGTVWINdYSVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
3-288 |
1.43e-110 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 327.60 E-value: 1.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07093 167 ANEAGLPPGVVNVVHGFGPEA-GAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07093 246 DAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATI 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGP----GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:cd07093 326 LTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVA 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 652636290 239 DGLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07093 406 RRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
5-288 |
3.85e-110 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 325.64 E-value: 3.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVE- 83
Cdd:cd07104 151 EAGLPKGVLNVVPG-GGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 84 GAMGAKMRNiGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:cd07104 230 AAFGAFLHQ-GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRvDGPgyFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07104 309 TGGTY-EGL--FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLET 385
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 244 GLMGFNSGVISNAA-APFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07104 386 GMVHINDQTVNDEPhVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
1-284 |
1.04e-107 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 319.41 E-value: 1.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVL-NVVAGKSASaisEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLD 79
Cdd:cd07100 144 ELFREAGFPEGVFqNLLIDSDQV---EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 80 EAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASG 159
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 160 ARAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSD 239
Cdd:cd07100 301 ATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 240 GLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQ 284
Cdd:cd07100 381 RLEAGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-288 |
6.97e-107 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 319.16 E-value: 6.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:PRK11241 199 AGIPAGVFNVVTG-SAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:PRK11241 278 LASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCG 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGL 245
Cdd:PRK11241 358 GKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGI 437
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 652636290 246 MGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:PRK11241 438 VGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
4-283 |
3.26e-105 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 314.53 E-value: 3.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 4 LDAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAAD-NVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07091 192 KEAGFPPGVVNIVPGFGPTA-GAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07091 271 EWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07091 351 LTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALK 430
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTV 283
Cdd:cd07091 431 AGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQV 471
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
6-283 |
5.90e-102 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 305.63 E-value: 5.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:cd07114 172 AGFPPGVVNVVTGFGPET-GEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:cd07114 251 VAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRRVDGP----GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGL 241
Cdd:cd07114 331 GERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAI 410
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 652636290 242 EFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTV 283
Cdd:cd07114 411 EAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQT 452
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
8-288 |
5.58e-101 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 302.91 E-value: 5.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMG 87
Cdd:cd07106 168 LPPGVLNVVSG--GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFW 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 88 AKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAGGR 167
Cdd:cd07106 246 GAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 168 RVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMG 247
Cdd:cd07106 326 PLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVW 405
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 652636290 248 FNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07106 406 INTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
5-286 |
5.33e-100 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 301.11 E-value: 5.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07088 185 EAGLPAGVLNIVTG-RGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07088 264 IVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDG-PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07088 344 GGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEF 423
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 244 GLMGFNSGvisNAAAPFG---GVKQSGLGREGGAEGLDEY--TTVQYI 286
Cdd:cd07088 424 GETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYlqTKVVYL 468
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
3-288 |
6.36e-97 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 293.45 E-value: 6.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07119 184 IEEAGLPAGVVNLVTG-SGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAV 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07119 263 DQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGP----GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:cd07119 343 VCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVA 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 652636290 239 DGLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07119 423 RRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1-286 |
2.17e-96 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 291.27 E-value: 2.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07115 165 ELMAEAGFPAGVLNVVTGFGEVA-GAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07115 244 AVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:cd07115 324 RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAA 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 241 LEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07115 404 LKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-286 |
7.20e-96 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 290.02 E-value: 7.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07110 172 EAGLPPGVLNVVTGT-GDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEW 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07110 251 AMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLC 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGP--GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07110 331 GGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07110 411 AGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
5-289 |
1.44e-95 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 289.59 E-value: 1.44e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07151 183 EAGLPKGVLNVVVGA-GSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07151 262 AVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLV 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVdgpGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFG 244
Cdd:cd07151 342 GGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAG 418
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 245 LMGFNSGVISNAA-APFGGVKQSGLGREGGAEGLDEYTTVQYIGIQ 289
Cdd:cd07151 419 MTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
7-286 |
4.42e-95 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 287.69 E-value: 4.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 7 GLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAM 86
Cdd:cd07092 171 VLPPGVVNVVCGGGASA-GDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 87 GAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAvASGARAVAGG 166
Cdd:cd07092 250 TAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA-PAHARVLTGG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 167 RRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLM 246
Cdd:cd07092 329 RRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTV 408
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 652636290 247 GFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07092 409 WVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
6-288 |
7.15e-95 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 287.60 E-value: 7.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:cd07089 176 TDLPAGVVNVVTG-SDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:cd07089 255 VGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRRVDG--PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07089 335 GGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRT 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 244 GLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07089 415 GSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-286 |
9.17e-95 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 287.96 E-value: 9.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMG 87
Cdd:PRK13473 192 LPPGVLNVVTGRGATV-GDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRT 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 88 AKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASG-ARAVAGG 166
Cdd:PRK13473 271 FGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 167 RRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLM 246
Cdd:PRK13473 351 EAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCT 430
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 652636290 247 GFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:PRK13473 431 WVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
5-286 |
2.70e-93 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 283.62 E-value: 2.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07138 182 EAGLPAGVFNLVNG-DGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPR 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESV---AEEFANKFAERISglnVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGAR 161
Cdd:cd07138 261 GVAACFANSGQSCNAPTRMLVPRSRyaeAEEIAAAAAEAYV---VGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGAR 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 162 AVAGGR-RVDGP--GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:cd07138 338 LVAGGPgRPEGLerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVA 417
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 239 DGLEFGLMGFNsGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07138 418 RRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
3-288 |
3.68e-93 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 283.07 E-value: 3.68e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07150 169 MEEAGLPKGVFNVVTG-GGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAM-GAKMRNiGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGAR 161
Cdd:cd07150 248 RAAAfGAFMHQ-GQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 162 AVAGGRRvDGPgyFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGL 241
Cdd:cd07150 327 LLTGGKY-DGN--FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERL 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 242 EFGLMGFN-SGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07150 404 ESGMVHINdPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
1-281 |
1.97e-92 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 281.41 E-value: 1.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAAD-NVLRTSMELGGNAPFIVFADA-DL 78
Cdd:cd07112 172 ELALEAGLPAGVLNVVPGFGHTA-GEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 79 DEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVAS 158
Cdd:cd07112 251 DAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 159 GARAVAGGRRV--DGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWR 236
Cdd:cd07112 331 GARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHR 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 237 LSDGLEFGLM---GFNSGVISnaaAPFGGVKQSGLGREGGAEGLDEYT 281
Cdd:cd07112 411 VARRLRAGTVwvnCFDEGDIT---TPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1-288 |
3.73e-92 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 280.27 E-value: 3.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07109 165 ELAEEAGLPAGALNVVTGLGAEA-GAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLdEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07109 244 ALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVARARARGA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDGP---GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRL 237
Cdd:cd07109 323 RIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRV 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 652636290 238 SDGLEFGLMGFNS-GVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07109 403 ARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
1-288 |
6.84e-90 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 274.61 E-value: 6.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSaSAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07145 171 KILEEAGLPPGVINVVTGYG-SEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07145 250 AVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDgpGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:cd07145 330 KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARE 407
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 652636290 241 LEFGLMGFN-SGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07145 408 LEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
5-288 |
1.66e-88 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 271.76 E-value: 1.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSAsaISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07139 189 EAGLPPGVVNVVPADRE--VGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07139 267 LVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVT 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGP--GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07139 347 GGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIR 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 243 FGLMGFNsGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07139 427 TGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-290 |
3.50e-88 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 271.37 E-value: 3.50e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:PRK13252 195 AGLPDGVFNVVQG--DGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:PRK13252 273 MLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRRVD----GPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGL 241
Cdd:PRK13252 353 GERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQL 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 652636290 242 EFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQ--YIGIQD 290
Cdd:PRK13252 433 EAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKsvQVEMGP 483
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
6-288 |
6.20e-87 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 267.25 E-value: 6.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:cd07090 169 AGLPDGVFNVVQG--GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:cd07090 247 MMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRRVDGP-----GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:cd07090 327 GERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQ 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 241 LEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07090 407 LQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
5-281 |
8.23e-87 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 267.74 E-value: 8.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAG---KSASAISEpimaDPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEA 81
Cdd:cd07144 196 EAGFPPGVVNIIPGygaVAGSALAE----HPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 82 VEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERI-SGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07144 272 VKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGG---RRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRL 237
Cdd:cd07144 352 KLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRV 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 238 SDGLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYT 281
Cdd:cd07144 432 ARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYT 475
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-288 |
1.25e-86 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 266.13 E-value: 1.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSAsAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07118 167 ELLIEAGLPAGVVNIVTGYGA-TVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDA 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07118 246 AADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVD-GPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSD 239
Cdd:cd07118 326 TLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVAR 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 652636290 240 GLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07118 406 RIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
5-286 |
2.04e-86 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 265.31 E-value: 2.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVE- 83
Cdd:cd07152 163 EAGLPAGVLHVLPG--GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASn 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 84 GAMGAKMRNiGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:cd07152 241 GAWGAFLHQ-GQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRvdgPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07152 320 AGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRT 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 244 GLMGFNSGVISNAA-APFGGVKQSGLG-REGGAEGLDEYTTVQYI 286
Cdd:cd07152 397 GMLHINDQTVNDEPhNPFGGMGASGNGsRFGGPANWEEFTQWQWV 441
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
3-287 |
4.38e-86 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 264.94 E-value: 4.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSASaISEPIMAdpRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07101 168 LIEAGLPRDLWQVVTGPGSE-VGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07101 245 AGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGR-RVD-GPgYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:cd07101 325 LAGGRaRPDlGP-YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAAR 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 652636290 241 LEFGLMGFNSGVIS---NAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIG 287
Cdd:cd07101 404 LRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
1-286 |
7.17e-86 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 264.46 E-value: 7.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAAdnVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07149 171 ELLLEAGLPKGALNVVTG-SGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07149 248 AVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVdgpGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:cd07149 328 RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARE 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 652636290 241 LEFGlmgfnsGVISNA-------AAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07149 405 LEVG------GVMINDsstfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
3-288 |
2.24e-85 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 263.07 E-value: 2.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07108 166 ILAQVLPAGVLNVITG-YGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMgAKMR--NIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVA-SG 159
Cdd:cd07108 245 DGAI-AGMRftRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLStSG 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 160 ARAVAGGRR----VDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMW 235
Cdd:cd07108 324 ATVLRGGPLpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRAL 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 652636290 236 RLSDGLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEG-LDEYTTVQYIGI 288
Cdd:cd07108 404 RAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
5-286 |
2.54e-85 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 262.93 E-value: 2.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSASAisePIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07099 171 AAGPPQGVLQVVTGDGATG---AALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07099 248 AVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFG 244
Cdd:cd07099 328 GGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAG 407
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 245 LMGFNSgVISNA---AAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07099 408 AVSIND-VLLTAgipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
6-283 |
2.20e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 260.83 E-value: 2.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGKSASAisEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:PRK09406 176 AGFPDGCFQTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:PRK09406 254 VTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGL 245
Cdd:PRK09406 334 GKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQ 413
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 652636290 246 MGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEY---TTV 283
Cdd:PRK09406 414 VFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFcniKTV 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
5-292 |
5.97e-84 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 260.82 E-value: 5.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:PLN02467 203 EVGLPPGVLNVVTGLGTEA-GAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEW 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:PLN02467 282 AMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILC 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDG--PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:PLN02467 362 GGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQ 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTV----QYIGiQDPY 292
Cdd:PLN02467 442 AGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVkqvtKYIS-DEPW 494
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-288 |
6.03e-84 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 260.07 E-value: 6.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSAsaISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07113 194 EAGIPDGVLNVVNGKGA--VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07113 272 LLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFG 244
Cdd:cd07113 352 GGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAG 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 245 LMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07113 432 TVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
5-288 |
8.61e-84 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 259.97 E-value: 8.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAAD-NVLRTSMELGGNAPFIVFADADLDEAVE 83
Cdd:cd07141 197 EAGFPPGVVNVVPGYGPTA-GAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 84 GAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:cd07141 276 QAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07141 356 CGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRA 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 244 GLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07141 436 GTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
1-288 |
8.64e-84 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 258.28 E-value: 8.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVV--AGKSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADL 78
Cdd:cd07105 146 RVFHEAGLPKGVLNVVthSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 79 DEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGdgldeDVTCGPLVEQKALDSVASLVDDAVAS 158
Cdd:cd07105 226 DAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 159 GARAVAGGRRVDGP-GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRL 237
Cdd:cd07105 301 GAKLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAV 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 652636290 238 SDGLEFGLMGFNSGVISN-AAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07105 381 AKRIESGAVHINGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
5-289 |
1.16e-83 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 257.36 E-value: 1.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:PRK10090 123 EIGLPKGVFNLVLGR-GETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLD-EDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:PRK10090 202 IVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:PRK10090 282 LGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKF 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 652636290 244 GLMGFNSgviSNAAAPFG---GVKQSGLGREGGAEGLDEYTTVQYIGIQ 289
Cdd:PRK10090 362 GETYINR---ENFEAMQGfhaGWRKSGIGGADGKHGLHEYLQTQVVYLQ 407
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-288 |
2.08e-83 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 258.81 E-value: 2.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADA-----DLDEAV 82
Cdd:cd07559 190 LPKGVVNVVTGF-GSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07559 269 EEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEV 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGP----GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:cd07559 349 LTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVA 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 652636290 239 DGLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07559 429 RGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
1-281 |
2.12e-83 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 258.82 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:cd07131 183 ELFAEAGLPPGVVNVVHGRGEEV-GEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07131 262 ALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDG----PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWR 236
Cdd:cd07131 342 TLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFR 421
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 652636290 237 LSDGLEFGLMGFNSGVI-SNAAAPFGGVKQSGLG-REGGAEGLDEYT 281
Cdd:cd07131 422 ARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFT 468
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
7-286 |
6.82e-83 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 256.89 E-value: 6.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 7 GLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAM 86
Cdd:cd07120 172 SLPAGVVNLFTE-SGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 87 GAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAGG 166
Cdd:cd07120 251 RALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 167 RRVDG---PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07120 331 GPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRA 410
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 652636290 244 GLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd07120 411 GTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
5-285 |
6.91e-83 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 257.49 E-value: 6.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07086 189 KNGLPPGVVNLVTG--GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07086 267 VLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLT 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDG--PGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRM--WRLSDG 240
Cdd:cd07086 347 GGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAfrWLGPKG 426
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 652636290 241 LEFGLMGFNSGVI-SNAAAPFGGVKQSGLGREGGAEGLDEYT-----TVQY 285
Cdd:cd07086 427 SDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYMrrstcTINY 477
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
3-289 |
1.12e-82 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 258.27 E-value: 1.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIM--ADprlrKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:PRK09407 204 LYEAGLPRDLWQVVTG-PGPVVGTALVdnAD----YLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:PRK09407 279 AAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGR-RVD-GPgYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:PRK09407 359 TVLAGGKaRPDlGP-LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIA 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 652636290 239 DGLEFGLMGFNSGVIS---NAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGIQ 289
Cdd:PRK09407 438 ARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQ 491
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-280 |
1.30e-82 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 256.94 E-value: 1.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07111 199 EAGLPPGVLNIVTG--NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07111 277 IVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQ 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFG 244
Cdd:cd07111 357 PGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAG 436
|
250 260 270
....*....|....*....|....*....|....*.
gi 652636290 245 LMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEY 280
Cdd:cd07111 437 VVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
5-288 |
5.17e-82 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 255.15 E-value: 5.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAA-DNVLRTSMELGGNAPFIVFADADLDEAVE 83
Cdd:cd07143 196 EAGFPPGVINVVSG-YGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAkSNLKKVTLELGGKSPNIVFDDADLESAVV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 84 GAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:cd07143 275 WTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07143 355 TGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKA 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 244 GLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07143 435 GTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
6-285 |
7.16e-82 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 255.11 E-value: 7.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAAD-NVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07140 200 AGFPKGVINILPG-SGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07140 279 GMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVY 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTE--QEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07140 359 GGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEY-----TTVQY 285
Cdd:cd07140 439 AGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYlktktVTIEY 486
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
5-283 |
1.21e-81 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 254.10 E-value: 1.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07097 187 EAGLPAGVFNLVMG-SGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVEC 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07097 266 AVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVY 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGP--GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07097 346 GGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVE 425
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 243 FGLMGFN---SGVISNaaAPFGGVKQSGLG-REGGAEGLDEYTTV 283
Cdd:cd07097 426 AGVVMVNlptAGVDYH--VPFGGRKGSSYGpREQGEAALEFYTTI 468
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
5-286 |
8.51e-81 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 248.68 E-value: 8.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd06534 144 EAGLPPGVVNVVPG-GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAerisglnvgdgldedvtcgplveqkaldsvaslvddavasgarava 164
Cdd:cd06534 223 AVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV---------------------------------------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 ggrrvdgpgyfyepTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFG 244
Cdd:cd06534 257 --------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAG 322
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 652636290 245 LMGFN-SGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYI 286
Cdd:cd06534 323 TVYINdSSIGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-288 |
1.31e-80 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 250.74 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLmkAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07146 170 LYEAGLPPDMLSVVTG-EPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07146 247 TLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVdgpGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07146 327 LLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLD 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 652636290 243 FGLM------GFNSGVIsnaaaPFGGVKQSGLG-REGGAEGLDEYTTVQYIGI 288
Cdd:cd07146 404 VGTVnvnevpGFRSELS-----PFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
5-283 |
1.01e-79 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 249.03 E-value: 1.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAAdnVLRTSMELGGNAPFIVFADADLDEAV-E 83
Cdd:cd07082 193 DAGFPKGVVNVVTGR-GREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAkE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 84 GAMGAKMRNiGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:cd07082 270 IVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRvDGPGYFYePTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07082 349 NGGGR-EGGNLIY-PTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEV 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 244 GLMGFNS------GVIsnaaaPFGGVKQSGLGREGGAEGLDEYTTV 283
Cdd:cd07082 427 GTVNINSkcqrgpDHF-----PFLGRKDSGIGTQGIGDALRSMTRR 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-288 |
5.44e-79 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 247.37 E-value: 5.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMG 87
Cdd:cd07117 190 LPKGVVNIVTGK-GSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 88 AKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAGGR 167
Cdd:cd07117 269 GILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGH 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 168 RVDGP----GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEF 243
Cdd:cd07117 349 RLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVET 428
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 652636290 244 GLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07117 429 GRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
4-284 |
4.04e-77 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 242.40 E-value: 4.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 4 LDAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLR-TSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07142 192 AEAGLPDGVLNIVTGFGPTA-GAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKpVTLELGGKSPFIVCEDADVDKAV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07142 271 ELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07142 351 ITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALK 430
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQ 284
Cdd:cd07142 431 AGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
8-289 |
1.59e-76 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 240.35 E-value: 1.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAM- 86
Cdd:cd07107 170 LPPGVFNILPGDGATA-GAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVa 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 87 GAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAGG 166
Cdd:cd07107 249 GMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 167 RRVDGP----GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07107 329 GRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVE 408
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGIQ 289
Cdd:cd07107 409 AGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
32-277 |
3.36e-76 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 239.89 E-value: 3.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 32 PRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAE 111
Cdd:cd07098 201 PVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 112 EFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAGGRRVDGP----GYFYEPTVLIDVPAD 187
Cdd:cd07098 281 KLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPD 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 188 ARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNSGVIS--NAAAPFGGVKQ 265
Cdd:cd07098 361 MKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKG 440
|
250
....*....|..
gi 652636290 266 SGLGREGGAEGL 277
Cdd:cd07098 441 SGFGRFAGEEGL 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
3-288 |
1.10e-75 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 238.10 E-value: 1.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSAsAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNvlRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07094 173 LVEAGVPEGVLQVVTGERE-VLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--RIALELGGNAPVIVDRDADLDAAI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07094 250 EALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRvdgPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07094 330 LCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLE 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 652636290 243 FGLMGFNSGVISNA-AAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:cd07094 407 VGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-284 |
7.65e-69 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 222.76 E-value: 7.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSASA---ISEPIMADprlrKVSFTGSTPVGKTLMKAAADNVLR-TSMELGGNAPFIVFADADL 78
Cdd:PLN02466 245 LHEAGLPPGVLNVVSGFGPTAgaaLASHMDVD----KLAFTGSTDTGKIVLELAAKSNLKpVTLELGGKSPFIVCEDADV 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 79 DEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVAS 158
Cdd:PLN02466 321 DKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVES 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 159 GARAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:PLN02466 401 GATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLS 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 239 DGLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQ 284
Cdd:PLN02466 481 RALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
6-281 |
1.30e-68 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 219.81 E-value: 1.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGKSAsaISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGA 85
Cdd:cd07102 169 AGLPEGVFQVLHLSHE--TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 86 MGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAG 165
Cdd:cd07102 247 VDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALID 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 166 GRR---VDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07102 327 GALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLE 406
|
250 260 270
....*....|....*....|....*....|....*....
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYT 281
Cdd:cd07102 407 TGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLT 445
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
3-281 |
2.83e-67 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 216.34 E-value: 2.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAgkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNvlRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07147 173 LAETGLPKGAFSVLP--CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07147 249 QRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRvDGPgyFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07147 329 LTGGKR-DGA--LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELE 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 243 FGlmgfnsGVISNA-------AAPFGGVKQSGLGREGGAEGLDEYT 281
Cdd:cd07147 406 VG------GVVINDvptfrvdHMPYGGVKDSGIGREGVRYAIEEMT 445
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
1-273 |
1.72e-65 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 213.24 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAA------DNVLRTSMELGGNAPFIVFA 74
Cdd:cd07124 214 EILEEAGLPPGVVNFLPG-PGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgqKWLKRVIAEMGGKNAIIVDE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 75 DADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDD 154
Cdd:cd07124 293 DADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 155 AVaSGARAVAGGRRVDGP--GYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPS 232
Cdd:cd07124 373 GK-SEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPE 451
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 233 RMWRLSDGLEFGLMGFNSGvISNA---AAPFGGVKQSGLGREGG 273
Cdd:cd07124 452 HLERARREFEVGNLYANRK-ITGAlvgRQPFGGFKMSGTGSKAG 494
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
6-284 |
3.58e-65 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 212.37 E-value: 3.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAG---KSASAISEPIMADprlrKVSFTGSTPVGKTLMKAAA-DNVLRTSMELGGNAPFIVFADADLDEA 81
Cdd:PLN02766 211 AGVPDGVINVVTGfgpTAGAAIASHMDVD----KVSFTGSTEVGRKIMQAAAtSNLKQVSLELGGKSPLLIFDDADVDMA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 82 VEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGAR 161
Cdd:PLN02766 287 VDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGAT 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 162 AVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGL 241
Cdd:PLN02766 367 LLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSI 446
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 652636290 242 EFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQ 284
Cdd:PLN02766 447 RAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-284 |
3.43e-64 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 208.56 E-value: 3.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSAsAISEPImADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDE 80
Cdd:PRK13968 174 QVFKDAGIPQGVYGWLNADND-GVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:PRK13968 252 AVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:PRK13968 332 RLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAAR 411
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 241 LEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQ 284
Cdd:PRK13968 412 LECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQ 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
8-280 |
1.46e-60 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 199.60 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFA------DADLDEA 81
Cdd:cd07116 190 LPPGVVNVVNGFGLEA-GKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFAdvmdadDAFFDKA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 82 VEG-AMGAkmRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGA 160
Cdd:cd07116 269 LEGfVMFA--LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRR----VDGPGYFYEPTVlIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWR 236
Cdd:cd07116 347 EVLTGGERnelgGLLGGGYYVPTT-FKGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYR 425
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 237 LSDGLEFGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEY 280
Cdd:cd07116 426 MGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHY 469
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
5-273 |
7.77e-60 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 197.43 E-value: 7.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEG 84
Cdd:cd07130 188 KNGLPGAIASLVCG--GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVA 164
Cdd:cd07130 266 VLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLF 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 165 GGRRVDGPGYFYEPTVlIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRM--WRLSDGLE 242
Cdd:cd07130 346 GGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAfrWLGPKGSD 424
|
250 260 270
....*....|....*....|....*....|...
gi 652636290 243 FGLMGFNSGViSNA--AAPFGGVKQSGLGREGG 273
Cdd:cd07130 425 CGIVNVNIGT-SGAeiGGAFGGEKETGGGRESG 456
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
5-288 |
5.32e-59 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 195.89 E-value: 5.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSASAiSEPIMADPRLRKVSFTGSTPVGKTLMKAAAD-NVLRTSMELGGNAPFIVFADA-DLDEAV 82
Cdd:PRK09847 209 EAGLPDGVLNVVTGFGHEA-GQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:PRK09847 288 SATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VaGGRRVDGPGYFyEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:PRK09847 368 L-DGRNAGLAAAI-GPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLK 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 652636290 243 FGLMGFNSGVISNAAAPFGGVKQSGLGREGGAEGLDEYTTVQYIGI 288
Cdd:PRK09847 446 AGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
3-267 |
1.32e-55 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 187.45 E-value: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADN------VLRTSMELGGNAPFIVFADA 76
Cdd:PRK03137 221 LEEAGLPAGVVNFVPG-SGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 77 DLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTcGPLVEQKALDSVASLVDDAV 156
Cdd:PRK03137 300 DLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYM-GPVINQASFDKIMSYIEIGK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 157 ASGaRAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWR 236
Cdd:PRK03137 379 EEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEK 457
|
250 260 270
....*....|....*....|....*....|....
gi 652636290 237 LSDGLEFGLMGFN---SGVISnAAAPFGGVKQSG 267
Cdd:PRK03137 458 ARREFHVGNLYFNrgcTGAIV-GYHPFGGFNMSG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
3-272 |
1.01e-53 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 181.08 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAgkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVlRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07148 174 LHEAGLPEGWCQAVP--CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT-RCALEHGGAAPVIVDRSADLDAMI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07148 251 PPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGPgyFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLE 242
Cdd:cd07148 331 LCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLD 408
|
250 260 270
....*....|....*....|....*....|....*..
gi 652636290 243 fglmgfNSGVISNAAA-------PFGGVKQSGLGREG 272
Cdd:cd07148 409 ------ATAVMVNDHTafrvdwmPFAGRRQSGYGTGG 439
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
1-273 |
3.17e-53 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 181.22 E-value: 3.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAA------DNVLRTSMELGGNAPFIVFA 74
Cdd:TIGR01237 215 EILEEAGLPKGVVQFVPG-SGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqKHLKRVIAEMGGKDTVIVDE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 75 DADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDD 154
Cdd:TIGR01237 294 DADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEI 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 155 AVASGaRAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRM 234
Cdd:TIGR01237 374 GKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHI 452
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 652636290 235 WRLSDGLEFGLMGFN---SGVISnAAAPFGGVKQSGLGREGG 273
Cdd:TIGR01237 453 NRAKAEFEVGNLYFNrniTGAIV-GYQPFGGFKMSGTDSKAG 493
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
3-281 |
1.32e-52 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 178.86 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAV 82
Cdd:cd07085 186 LQEAGLPDGVLNVVHG--GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 EGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARA 162
Cdd:cd07085 264 NALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 163 VAGGRRVDGPGY----FYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:cd07085 344 VLDGRGVKVPGYengnFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQ 423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 652636290 239 DGLEFGLMGFNSGVisnaAAP-----FGGVKQSGLGREG--GAEGLDEYT 281
Cdd:cd07085 424 REVDAGMVGINVPI----PVPlaffsFGGWKGSFFGDLHfyGKDGVRFYT 469
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
39-281 |
1.74e-51 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 174.72 E-value: 1.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 39 FTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFA 118
Cdd:cd07134 182 FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLK 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 119 ERIsGLNVGDGLDEDVTC--GPLVEQKALDSVASLVDDAVASGARAVAGGRRVDGPGYFYePTVLIDVPADARVVQEEIF 196
Cdd:cd07134 262 AEI-EKFYGKDAARKASPdlARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIA-PTVLTNVTPDMKIMQEEIF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 197 GPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNSGVI--SNAAAPFGGVKQSGLGREGGA 274
Cdd:cd07134 340 GPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhfLNPNLPFGGVNNSGIGSYHGV 419
|
....*..
gi 652636290 275 EGLDEYT 281
Cdd:cd07134 420 YGFKAFS 426
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
39-281 |
1.36e-50 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 172.33 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 39 FTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFA 118
Cdd:cd07087 182 FTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELK 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 119 ERISGLnVGDGLDEDVTCGPLVEQKALDSVASLVDDavasgARAVAGGrRVDGPGYFYEPTVLIDVPADARVVQEEIFGP 198
Cdd:cd07087 262 KAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDD-----GKVVIGG-QVDKEERYIAPTILDDVSPDSPLMQEEIFGP 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 199 VAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNSGVI--SNAAAPFGGVKQSGLGREGGAEG 276
Cdd:cd07087 335 ILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVGNSGMGAYHGKAG 414
|
....*
gi 652636290 277 LDEYT 281
Cdd:cd07087 415 FDTFS 419
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
1-273 |
1.04e-47 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 164.75 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRT-SMELGGNAPFIVFADADLD 79
Cdd:cd07095 145 ELWEEAGLPPGVLNLVQG--GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADID 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 80 EAVEGAMGAKMRNIGEACTAANRFIVHES-VAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVAS 158
Cdd:cd07095 223 AAAYLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLAL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 159 GARAVAGGRRVDGPGYFYEPTvLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:cd07095 303 GGEPLLAMERLVAGTAFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
|
250 260 270
....*....|....*....|....*....|....*...
gi 652636290 239 DGLEFGLMGFN---SGviSNAAAPFGGVKQSGLGREGG 273
Cdd:cd07095 382 ARIRAGIVNWNrptTG--ASSTAPFGGVGLSGNHRPSA 417
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
39-281 |
1.54e-47 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 164.20 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 39 FTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFA 118
Cdd:cd07133 183 FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 119 ERISGLnVGDGLD-EDVTCgpLVEQKALDSVASLVDDAVASGARAV---------AGGRRvdgpgyfYEPTVLIDVPADA 188
Cdd:cd07133 263 AAVAKM-YPTLADnPDYTS--IINERHYARLQGLLEDARAKGARVIelnpagedfAATRK-------LPPTLVLNVTDDM 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 189 RVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNsGVISNAA---APFGGVKQ 265
Cdd:cd07133 333 RVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN-DTLLHVAqddLPFGGVGA 411
|
250
....*....|....*.
gi 652636290 266 SGLGREGGAEGLDEYT 281
Cdd:cd07133 412 SGMGAYHGKEGFLTFS 427
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
39-281 |
6.59e-44 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 154.97 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 39 FTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFA 118
Cdd:cd07136 182 FTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELK 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 119 ERISGLNVGDGLDEDvTCGPLVEQKALDSVASLVDDAvasgaRAVAGGRrVDGPGYFYEPTVLIDVPADARVVQEEIFGP 198
Cdd:cd07136 262 EEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----KIVFGGN-TDRETLYIEPTILDNVTWDDPVMQEEIFGP 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 199 VAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGlmgfnSGVI-------SNAAAPFGGVKQSGLGRE 271
Cdd:cd07136 335 ILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFG-----GGCIndtimhlANPYLPFGGVGNSGMGSY 409
|
250
....*....|
gi 652636290 272 GGAEGLDEYT 281
Cdd:cd07136 410 HGKYSFDTFS 419
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
36-281 |
8.48e-43 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 151.99 E-value: 8.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 36 KVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFAN 115
Cdd:cd07135 187 KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 116 KFAERISGLnVGDGLDEDVTCGPLVEQKALDSVASLVDDavaSGARAVAGGRRvDGPGYFYEPTVLIDVPADARVVQEEI 195
Cdd:cd07135 267 ELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEM-DEATRFIPPTIVSDVSWDDSLMSEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 196 FGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNSGVI--SNAAAPFGGVKQSGLGREGG 273
Cdd:cd07135 342 FGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSGYGAYHG 421
|
....*...
gi 652636290 274 AEGLDEYT 281
Cdd:cd07135 422 KYGFDTFT 429
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
7-280 |
5.03e-42 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 151.14 E-value: 5.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 7 GLPAGVLNVVAGksASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAM 86
Cdd:PLN02315 212 NLPGAIFTSFCG--GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 87 GAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAVAGG 166
Cdd:PLN02315 290 FAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGG 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 167 RRVDGPGYFYEPTVlIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRM--WRLSDGLEFG 244
Cdd:PLN02315 370 SAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIfkWIGPLGSDCG 448
|
250 260 270
....*....|....*....|....*....|....*....
gi 652636290 245 LMGFNsgVISNAA---APFGGVKQSGLGREGGAEGLDEY 280
Cdd:PLN02315 449 IVNVN--IPTNGAeigGAFGGEKATGGGREAGSDSWKQY 485
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
39-281 |
1.26e-41 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 149.79 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 39 FTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFA 118
Cdd:PTZ00381 191 FTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 119 ERISGLnVGDGLDEDVTCGPLVEQKALDSVASLVDDavaSGARAVAGGrRVDGPGYFYEPTVLIDVPADARVVQEEIFGP 198
Cdd:PTZ00381 271 EAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGG-EVDIENKYVAPTIIVNPDLDSPLMQEEIFGP 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 199 VAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNSGV--ISNAAAPFGGVKQSGLGREGGAEG 276
Cdd:PTZ00381 346 ILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGVGNSGMGAYHGKYG 425
|
....*
gi 652636290 277 LDEYT 281
Cdd:PTZ00381 426 FDTFS 430
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-272 |
5.78e-41 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 147.98 E-value: 5.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKsASAISEPIMADPRLRKVSFTGSTpVGKTLMKAAAdnVLRTSMELGGNAPFIVFADADLDE 80
Cdd:PLN00412 206 HCFHLAGFPKGLISCVTGK-GSEIGDFLTMHPGVNCISFTGGD-TGIAISKKAG--MVPLQMELGGKDACIVLEDADLDL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 81 AVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDE-DVTcgPLVEQKALDSVASLVDDAVASG 159
Cdd:PLN00412 282 AAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDcDIT--PVVSESSANFIEGLVMDAKEKG 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 160 ARAVAGGRRvdgPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSD 239
Cdd:PLN00412 360 ATFCQEWKR---EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISD 436
|
250 260 270
....*....|....*....|....*....|....*....
gi 652636290 240 GLEFGLMGFNSgvisnAAA------PFGGVKQSGLGREG 272
Cdd:PLN00412 437 AMETGTVQINS-----APArgpdhfPFQGLKDSGIGSQG 470
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
5-286 |
4.49e-40 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 145.80 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSASaISEPIMADPRLRKVSFTGSTPVGKTLMKAAADN------VLRTSMELGGNAPFIVFADADL 78
Cdd:cd07083 206 EAGFPPGVVQFLPGVGEE-VGAYLTEHERIRGINFTGSLETGKKIYEAAARLapgqtwFKRLYVETGGKNAIIVDETADF 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 79 DEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVAS 158
Cdd:cd07083 285 ELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 159 GaRAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQ--EAITLANATEYGLASYVFTEDPSRMWR 236
Cdd:cd07083 365 G-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEE 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 652636290 237 LSDGLEFGLMGFNSGVISNAAA--PFGGVKQSGLG-REGGAEGLDEYTTVQYI 286
Cdd:cd07083 444 ARREFHVGNLYINRKITGALVGvqPFGGFKLSGTNaKTGGPHYLRRFLEMKAV 496
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
1-267 |
2.09e-37 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 138.87 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVL------RTSMELGGNAPFIVFA 74
Cdd:cd07123 217 KILEEAGLPPGVINFVPG-DGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 75 DADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDD 154
Cdd:cd07123 296 SADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 155 AVAS-GARAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLA---NATEYGLASYVFTED 230
Cdd:cd07123 376 AKSDpEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLElvdTTSPYALTGAIFAQD 455
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 652636290 231 PSRMWRLSDGLEF--GLMGFN---SGVISnAAAPFGGVKQSG 267
Cdd:cd07123 456 RKAIREATDALRNaaGNFYINdkpTGAVV-GQQPFGGARASG 496
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
1-286 |
6.73e-35 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 132.22 E-value: 6.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSAsAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVL------RTSMELGGNAPFIVFA 74
Cdd:TIGR01236 216 RILEEAGLPPGVINFVPGDGV-QVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDryhnfpRIVGETGGKDFHLVHP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 75 DADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDD 154
Cdd:TIGR01236 295 SADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIED 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 155 AVASGAR--AVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLA---NATEYGLASYVFTE 229
Cdd:TIGR01236 375 AKKDPEAltILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDlvdSTSQYGLTGAVFAK 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 652636290 230 DPSRMWRLSDGLEFGLMGF-----NSGVISnAAAPFGGVKQSGLG-REGGAEGLDEYTTVQYI 286
Cdd:TIGR01236 455 DRKAILEADKKLRFAAGNFyindkCTGAVV-GQQPFGGARMSGTNdKAGGPNNLLRWTSPRSI 516
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
36-281 |
4.05e-34 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 128.68 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 36 KVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKM-RNIGEACTAANRFIVHESVAEEFA 114
Cdd:cd07137 180 KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLI 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 115 NKFAERISGLnVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASgARAVAGGRRvDGPGYFYEPTVLIDVPADARVVQEE 194
Cdd:cd07137 260 DALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGER-DEKNLYIEPTILLDPPLDSSIMTEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 195 IFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNSGVI--SNAAAPFGGVKQSGLGREG 272
Cdd:cd07137 337 IFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqyAIDTLPFGGVGESGFGAYH 416
|
....*....
gi 652636290 273 GAEGLDEYT 281
Cdd:cd07137 417 GKFSFDAFS 425
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
33-281 |
5.33e-34 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 128.49 E-value: 5.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 33 RLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEE 112
Cdd:cd07132 176 RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 113 FANKFAERISGLnVGDGLDEDVTCGPLVEQKALDSVASLVddavaSGARAVAGGRrVDGPGYFYEPTVLIDVPADARVVQ 192
Cdd:cd07132 256 FVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 193 EEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDGLEFGLMGFNSGVISNAAA--PFGGVKQSGLGR 270
Cdd:cd07132 329 EEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDslPFGGVGNSGMGA 408
|
250
....*....|.
gi 652636290 271 EGGAEGLDEYT 281
Cdd:cd07132 409 YHGKYSFDTFS 419
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
4-289 |
3.87e-32 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 124.86 E-value: 3.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 4 LDAGLPAGVLNVVAGKSASAisEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEAVE 83
Cdd:PLN02419 300 MEAGLPDGVLNIVHGTNDTV--NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLN 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 84 GAMGAKMRNIGEACTAANRfIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGARAV 163
Cdd:PLN02419 378 ALLAAGFGAAGQRCMALST-VVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 164 AGGRRVDGPGY----FYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSD 239
Cdd:PLN02419 457 LDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQM 536
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 652636290 240 GLEFGLMGFNSGV-ISNAAAPFGGVKQSGLGREG--GAEGLDEYTTVQYIGIQ 289
Cdd:PLN02419 537 DIEAGQIGINVPIpVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIKLVTQK 589
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
5-267 |
4.87e-30 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 118.14 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSASAISepIMADPRLRKVSFTGSTPVGKTLMKAAA---DNVLrtSMELGGNAPFIVFADADLDEA 81
Cdd:PRK09457 186 QAGLPAGVLNLVQGGRETGKA--LAAHPDIDGLLFTGSANTGYLLHRQFAgqpEKIL--ALEMGGNNPLVIDEVADIDAA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 82 VEGAMGAKMRNIGEACTAANRFIVHESV-AEEFANKFAERISGLNVGDgLDEDVT--CGPLVEQKALDSVASLVDDAVAS 158
Cdd:PRK09457 262 VHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGR-WDAEPQpfMGAVISEQAAQGLVAAQAQLLAL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 159 GARAVAGGRRVDGPGYFYEPTvLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLS 238
Cdd:PRK09457 341 GGKSLLEMTQLQAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL 419
|
250 260 270
....*....|....*....|....*....|..
gi 652636290 239 DGLEFGLMGFN---SGVISnaAAPFGGVKQSG 267
Cdd:PRK09457 420 LEIRAGIVNWNkplTGASS--AAPFGGVGASG 449
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-273 |
5.73e-30 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 118.07 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSASaISEPIMADPRLRKVSFTGSTPVGKTLMKAAADN---VLRTSMELGG-NApFIVFADA 76
Cdd:cd07125 215 ELLHEAGVPRDVLQLVPGDGEE-IGEALVAHPRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGkNA-MIVDSTA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 77 DLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAV 156
Cdd:cd07125 293 LPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMR 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 157 ASgARAVAGGRRVDGPGYFYEPTVLIDVPADarVVQEEIFGPVAPVITFSTEQ--EAITLANATEYGLASYVFTEDPSRM 234
Cdd:cd07125 373 GE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEDldEAIEDINATGYGLTLGIHSRDEREI 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 235 WRLSDGLEFGLMGFNSGVIsnaAA-----PFGGVKQSGLGREGG 273
Cdd:cd07125 450 EYWRERVEAGNLYINRNIT---GAivgrqPFGGWGLSGTGPKAG 490
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
8-281 |
3.81e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 115.59 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGksASAISEPIMaDPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIV---FADADLDEAVEG 84
Cdd:PLN02203 162 LDSKAVKVIEG--GPAVGEQLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 AMGAKMRNI-GEACTAANRFIVHESVAE---EFANKFAERISGLNVgdglDEDVTCGPLVEQKALDSVASLVDD-AVASg 159
Cdd:PLN02203 239 IVGGKWGSCaGQACIAIDYVLVEERFAPiliELLKSTIKKFFGENP----RESKSMARILNKKHFQRLSNLLKDpRVAA- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 160 arAVAGGRRVDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSD 239
Cdd:PLN02203 314 --SIVHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILS 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 652636290 240 GLEFGLMGFNSGVISNA--AAPFGGVKQSGLGREGGAEGLDEYT 281
Cdd:PLN02203 392 ETSSGSVTFNDAIIQYAcdSLPFGGVGESGFGRYHGKYSFDTFS 435
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
3-281 |
1.84e-24 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 102.43 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGksasAISE-PIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTSMELGGNAPFIVFADADLDEA 81
Cdd:PLN02174 161 LLEQYLDSSAVRVVEG----AVTEtTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 82 VEGAMGAKMR-NIGEACTAANRFIVHESVAEEFANKFAERISGLnVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASGa 160
Cdd:PLN02174 237 VRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSD- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRvDGPGYFYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYVFTEDPSRMWRLSDG 240
Cdd:PLN02174 315 KIVYGGEK-DRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAAT 393
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 652636290 241 LEFGLMGFNSGVISNA--AAPFGGVKQSGLGREGGAEGLDEYT 281
Cdd:PLN02174 394 VSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFS 436
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
1-231 |
3.34e-21 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 93.10 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAG-LPAGVLNVVAGKSASAISEPIMADprlrKVSFTGSTPVGKTLmkAAADNVLRTSmelggnAPFIVFADAdLD 79
Cdd:cd07128 192 KDIVESGlLPEGALQLICGSVGDLLDHLGEQD----VVAFTGSAATAAKL--RAHPNIVARS------IRFNAEADS-LN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 80 EAVEGA-------------------MGAKMrniGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLV 140
Cdd:cd07128 259 AAILGPdatpgtpefdlfvkevareMTVKA---GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 141 EQKALDSVASLVdDAVASGARAVAGGRRVDGP-------GYFYEPTVLI-DVPADARVVQE-EIFGPVAPVITFSTEQEA 211
Cdd:cd07128 336 SREQREDVRAAV-ATLLAEAEVVFGGPDRFEVvgadaekGAFFPPTLLLcDDPDAATAVHDvEAFGPVATLMPYDSLAEA 414
|
250 260
....*....|....*....|
gi 652636290 212 ITLANATEYGLASYVFTEDP 231
Cdd:cd07128 415 IELAARGRGSLVASVVTNDP 434
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
4-241 |
1.18e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 85.53 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 4 LDAG-LPAGVLNVVAGKSASAISEPIMADprlrKVSFTGSTPVGKTL--MKAAADNVLRTSMELGGNAPFIVFADADLD- 79
Cdd:PRK11903 199 VAAGiLPAGALSVVCGSSAGLLDHLQPFD----VVSFTGSAETAAVLrsHPAVVQRSVRVNVEADSLNSALLGPDAAPGs 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 80 EAVEGAMGAKMRNI----GEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSV-ASLvdD 154
Cdd:PRK11903 275 EAFDLFVKEVVREMtvksGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVrAGL--A 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 155 AVASGARAVAGGRRV------DGPGYFYEPTVLI--DVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGLASYV 226
Cdd:PRK11903 353 ALRAQAEVLFDGGGFalvdadPAVAACVGPTLLGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASV 432
|
250
....*....|....*
gi 652636290 227 FTEDPSRMWRLSDGL 241
Cdd:PRK11903 433 YSDDAAFLAAAALEL 447
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
3-285 |
7.66e-17 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 80.34 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSASaISEPIMADPRLRKVSFTGSTPVGKTLMKAAA---DNVLRTSMELGGNAPFIVFADADLD 79
Cdd:TIGR01238 210 MQEAGFPAGTIQLLPGRGAD-VGAALTSDPRIAGVAFTGSTEVAQLINQTLAqreDAPVPLIAETGGQNAMIVDSTALPE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 80 EAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVGDGLDEDVTCGPLVEQKALDSVASLVDDAVASG 159
Cdd:TIGR01238 289 QVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQ 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 160 ---ARAVAGGRRVDGPGYFYEPTVL-IDvpaDARVVQEEIFGPVAPVITFSTEQ--EAITLANATEYGLASYVFTEDPSR 233
Cdd:TIGR01238 369 kkiAQLTLDDSRACQHGTFVAPTLFeLD---DIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETT 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 652636290 234 MWRLSDGLEFGLMGFNSGVISNAAA--PFGGVKQSGLG-REGGAEGLDEYTTVQY 285
Cdd:TIGR01238 446 YRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTGpKAGGPHYLYRLTQVQY 500
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
3-222 |
9.96e-14 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 71.43 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGkSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNvlrtsmeLGGNAPFI----------V 72
Cdd:PRK11905 726 LHEAGVPKDALQLLPG-DGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKR-------SGPPVPLIaetggqnamiV 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 73 FADADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEefanKFAERISG----LNVGDG--LDEDVtcGPLVEQKALD 146
Cdd:PRK11905 798 DSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVAD----RVLTMLKGamdeLRIGDPwrLSTDV--GPVIDAEAQA 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 147 SVASLVDDAVASGAR--AVAGGRRVDGpGYFYEPTvLIDVPaDARVVQEEIFGPVAPVITFSTEQ-----EAItlaNATE 219
Cdd:PRK11905 872 NIEAHIEAMRAAGRLvhQLPLPAETEK-GTFVAPT-LIEID-SISDLEREVFGPVLHVVRFKADEldrviDDI---NATG 945
|
...
gi 652636290 220 YGL 222
Cdd:PRK11905 946 YGL 948
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
6-219 |
2.66e-12 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 66.80 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 6 AGLPAGVLNVVAGKSaSAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADnvlRTS-----MELGGNAPFIVFADA---D 77
Cdd:cd07129 164 TGLPAGVFSLLQGGG-REVGVALVKHPAIKAVGFTGSRRGGRALFDAAAA---RPEpipfyAELGSVNPVFILPGAlaeR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 78 LDEAVEGAMGAKMRNIGEACTAANRFIVHESVA-EEFANKFAERISGLNVGDGLDEDVtcgplveQKALDS-VASLVDda 155
Cdd:cd07129 240 GEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTMLTPGI-------AEAYRQgVEALAA-- 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 652636290 156 vASGARAVAGGrRVDGPGYFYEPTVLIDVPADAR---VVQEEIFGPVAPVITFSTEQEAITLANATE 219
Cdd:cd07129 311 -APGVRVLAGG-AAAEGGNQAAPTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
3-222 |
3.44e-12 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 66.76 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSAsAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADnvlRTS------MELGG-NApFIVFAD 75
Cdd:PRK11904 734 LHEAGIPKDVLQLLPGDGA-TVGAALTADPRIAGVAFTGSTETARIINRTLAA---RDGpivpliAETGGqNA-MIVDST 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 76 ADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEefanKFAERISG----LNVGDGLDEDVTCGPLVEQKALDSVASL 151
Cdd:PRK11904 809 ALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIAD----RVIEMLKGamaeLKVGDPRLLSTDVGPVIDAEAKANLDAH 884
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 652636290 152 VdDAVASGARAVAGGRRVDGP--GYFYEPTVL-IDvpaDARVVQEEIFGPVAPVITFSTEQ-----EAItlaNATEYGL 222
Cdd:PRK11904 885 I-ERMKREARLLAQLPLPAGTenGHFVAPTAFeID---SISQLEREVFGPILHVIRYKASDldkviDAI---NATGYGL 956
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
3-222 |
4.30e-11 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 63.42 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSASaISEPIMADPRLRKVSFTGSTPVGKTLMKAAADnvlRTSM------ELGG-NApFIVFAD 75
Cdd:COG4230 730 LHEAGVPADVLQLLPGDGET-VGAALVADPRIAGVAFTGSTETARLINRTLAA---RDGPivpliaETGGqNA-MIVDSS 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 76 ADLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEefanKFAERISG----LNVGDGLDEDVTCGPLVEQKALDSVASL 151
Cdd:COG4230 805 ALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIAD----RVLEMLKGamaeLRVGDPADLSTDVGPVIDAEARANLEAH 880
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 652636290 152 VdDAVASGARAVAGGRRVDGP--GYFYEPTvLIDVPaDARVVQEEIFGPVAPVITFSTEQ-----EAItlaNATEYGL 222
Cdd:COG4230 881 I-ERMRAEGRLVHQLPLPEECanGTFVAPT-LIEID-SISDLEREVFGPVLHVVRYKADEldkviDAI---NATGYGL 952
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
3-273 |
8.05e-11 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 62.68 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVAGKSASaISEPIMADPRLRKVSFTGSTPVGKTLMKAAA---DNVLRTS---MELGGNAPFIVFADA 76
Cdd:PRK11809 818 LLEAGVPAGVVQLLPGRGET-VGAALVADARVRGVMFTGSTEVARLLQRNLAgrlDPQGRPIpliAETGGQNAMIVDSSA 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 77 DLDEAVEGAMGAKMRNIGEACTAANRFIVHESVAEEFANKFAERISGLNVG--DGLDEDVtcGPLVEQKALDSVASLVDD 154
Cdd:PRK11809 897 LTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGnpDRLSTDI--GPVIDAEAKANIERHIQA 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 155 AVASG---ARAVAGGRRVDGPGYFYEPTvLIDVPADARvVQEEIFGPVAPVITFSTEQ-----EAItlaNATEYGLASYV 226
Cdd:PRK11809 975 MRAKGrpvFQAARENSEDWQSGTFVPPT-LIELDSFDE-LKREVFGPVLHVVRYNRNQldeliEQI---NASGYGLTLGV 1049
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 652636290 227 FTEDPSRMWRLSDGLEFGLMGFNSGVISNAAA--PFGGVKQSGLGREGG 273
Cdd:PRK11809 1050 HTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTGPKAG 1098
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
8-242 |
5.17e-10 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 59.56 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 8 LPAGVLNVVAGKSASaiSEPIMADPRLRKVSFTGSTPVGKTLMKAAADnvLRTSMELGGNAPFIVFADADLDEAVEGAMG 87
Cdd:cd07084 156 LPPEDVTLINGDGKT--MQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQAVDYVAWQCV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 88 AKMR-NIGEACTAANRFIVHES-----VAEEFANKFAERI-SGLNVGDGLDEDVtcgplveQKALDSVASLVDDAVASGA 160
Cdd:cd07084 232 QDMTaCSGQKCTAQSMLFVPENwsktpLVEKLKALLARRKlEDLLLGPVQTFTT-------LAMIAHMENLLGSVLLFSG 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 161 RAVAGGRRVDGPGYFYEPTVLIDVPADAR---VVQEEIFGPVAPVITFSTEQEAITLANAT-EYG-LASYVFTEDPSRMW 235
Cdd:cd07084 305 KELKNHSIPSIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLALVLELLErMHGsLTAAIYSNDPIFLQ 384
|
....*..
gi 652636290 236 RLSDGLE 242
Cdd:cd07084 385 ELIGNLW 391
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
5-274 |
3.90e-06 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 47.86 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 5 DAGLPAGVLNVVAGKSASAISEPIMADPRLRKVSFTGSTPVGKTLMKAAADNVLRTsmELGGNAPFIVFADADLDeaveg 84
Cdd:cd07127 249 EAGFDPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVYT--EKAGVNTVVVDSTDDLK----- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 85 amgAKMRNI--------GEACTAANRFIV----------HESvAEEFANKFAERISGLnVGDGLDEDVTCGPLVEQKALD 146
Cdd:cd07127 322 ---AMLRNLafslslysGQMCTTPQNIYVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 147 SVAslvddAVASGARAVAGGRRVDGPGY----FYEPTVLIDVPADARVVQEEIFGPVAPVITFSTEQEAITLANAT--EY 220
Cdd:cd07127 397 RIA-----EARQLGEVLLASEAVAHPEFpdarVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEH 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 652636290 221 G-LASYVFTEDPSRMWRLSD-GLEFGL---MGFNSGVISNAAAPFGGVKQSGLGREGGA 274
Cdd:cd07127 472 GaMTVGVYSTDPEVVERVQEaALDAGValsINLTGGVFVNQSAAFSDFHGTGANPAANA 530
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
3-214 |
1.11e-04 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 43.25 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 3 MLDAGLPAGVLNVVagKSASAISEPIMADPRLRKVSFTGSTPVGKTLmkaaadnvlrtSMELGGNapfIVFADADLDEAV 82
Cdd:cd07126 192 LHLCGMPATDVDLI--HSDGPTMNKILLEANPRMTLFTGSSKVAERL-----------ALELHGK---VKLEDAGFDWKI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 83 egaMGAKMRNI---------------GEACTAANRFIVHES-VAEEFANKFAERISGLNVgdgldEDVTCGPLV---EQK 143
Cdd:cd07126 256 ---LGPDVSDVdyvawqcdqdayacsGQKCSAQSILFAHENwVQAGILDKLKALAEQRKL-----EDLTIGPVLtwtTER 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 144 ALDSVASLvddAVASGARAVAGGRRVDG---PGYF--YEPTVL------IDVPADARVVQEEIFGPVAPVITFSTEQEAI 212
Cdd:cd07126 328 ILDHVDKL---LAIPGAKVLFGGKPLTNhsiPSIYgaYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLPL 404
|
..
gi 652636290 213 TL 214
Cdd:cd07126 405 VL 406
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
1-222 |
2.27e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 42.20 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 1 QTMLDAGLPAGVLNVVAGKSASAISEpIMADPRLRKVSFTGSTPVGKTLMK-------AAAdnvlrtsmelgGNAPFIVF 73
Cdd:PRK15398 181 EAIVAAGGPENLVVTVAEPTIETAQR-LMKHPGIALLVVTGGPAVVKAAMKsgkkaigAGA-----------GNPPVVVD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652636290 74 ADADLDEA----VEGAmgAKMRNIgeACTAANRFIVHESVAEEFANKFaERISGLNVGDGLDEDVTcgplveQKALDSVA 149
Cdd:PRK15398 249 ETADIEKAardiVKGA--SFDNNL--PCIAEKEVIVVDSVADELMRLM-EKNGAVLLTAEQAEKLQ------KVVLKNGG 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 652636290 150 SLVDDAVASGARAVAGGRRVDGPGyfyEPTVLI-DVPADARVVQEEIFGPVAPVITFSTEQEAITLANATEYGL 222
Cdd:PRK15398 318 TVNKKWVGKDAAKILEAAGINVPK---DTRLLIvETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGN 388
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
74-126 |
3.27e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 38.51 E-value: 3.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 652636290 74 ADADLDEAVEGAMGAKMRNIGeACTAANRFIVHESVAEEFANKFAERISGLNV 126
Cdd:PRK00197 235 ESADLDKALKIVLNAKTQRPS-VCNALETLLVHEAIAEEFLPKLAEALAEAGV 286
|
|
| |
